Advancing technologies often rely on concentrated or purified materials. As such, there continues to be a need to improve concentration and purification devices and methods. Commonly used purification methods for recovering and purifying protein include: Ion-exchange chromatography separates proteins with differences in charge and has high sample loading capacity. The separation is based on the reversible interaction between a charged protein and an oppositely charged chromatographic medium; Size-exclusion chromatography is a separation technique based on the molecular size of the components. Separation is achieved by the differential exclusion from the pores of the packing material, of the sample molecules as they pass through a bed of porous particles; hydrophobic interaction chromatography separates proteins with differences in hydrophobicity. The separation is based on the reversible interaction between a protein and the hydrophobic surface of a chromatographic medium; affinity chromatography separates molecules based on the reversible interaction between target protein and the specific ligand attached to a chromatography matrix; aqueous phase separation is an aqueous, liquid-liquid, biphasic system which is obtained either by mixture of aqueous solution of two polymers, or a polymer and a salt. Generally, the former aqueous is comprised of PEG and polymers like dextran, starch, polyvinylalcohol, etc. The latter one is composed of PEG and phosphate or sulphate salts; and self-cleaving affinity tag with low-cost resin combine self-cleaving affinity tag with the low-cost affinity resin (i.e., polyhydroxybutyrate (PHB) matrix, polyhydroxyalkanoates (PHA) granules, and cellulose binding module (CMB)). However, these devices and techniques have limitations and disadvantages.